Evidence map›Paper›PMID 40921734›Full record

ArticleNature cell biology2025

Hbo1 and Msl complexes preserve differential compaction and H3K27me3 marking of active and inactive X chromosomes during mitosis.

Dounia Djeghloul, Sherry Cheriyamkunnel, Bhavik Patel, Holger Kramer, Alex Montoya, Karen E Brown, Chad Whilding, Tatyana B Nesterova, Guifeng Wei, Neil Brockdorff and 5 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature cell biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Review
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

15 authors.

Dounia Djeghloul *Department of Biochemistry, University of Oxford, Oxford, UK. dounia-zede.djeghloul@cnrs.fr.ORCID http://orcid.org/0000-0002-7914-9777
Sherry Cheriyamkunnel *Epigenetic Memory Group, MRC Laboratory of Medical Sciences, Faculty of Medicine, Imperial College London, London, UK.
Bhavik PatelFlow Cytometry Facility, MRC Laboratory of Medical Sciences, Faculty of Medicine, Imperial College London, London, UK.
Holger KramerMass spectrometry Facility, MRC Laboratory of Molecular Biology, Cambridge, UK.ORCID http://orcid.org/0000-0002-6400-0945
Alex MontoyaProteomics and Metabolomics Facility, MRC Laboratory of Medical Sciences, Faculty of Medicine, Imperial College London, London, UK.ORCID http://orcid.org/0000-0002-6501-883X
Karen E BrownEpigenetic Memory Group, MRC Laboratory of Medical Sciences, Faculty of Medicine, Imperial College London, London, UK.
Chad WhildingMicroscopy Facility, MRC Laboratory of Medical Sciences, Faculty of Medicine, Imperial College London, London, UK.
Tatyana B NesterovaDepartment of Biochemistry, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0001-7740-4386
Guifeng WeiDepartment of Biochemistry, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-5698-426X
Neil BrockdorffDepartment of Biochemistry, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0003-4838-2653
Iga GrządzielewskaMax-Planck Institute of Immunobiology and Epigenetics, Freiburg, Germany.
Remzi KarayolMax-Planck Institute of Immunobiology and Epigenetics, Freiburg, Germany.
Asifa AkhtarMax-Planck Institute of Immunobiology and Epigenetics, Freiburg, Germany.ORCID http://orcid.org/0000-0001-8973-6193
Matthias MerkenschlagerLymphocyte Development Group, MRC Laboratory of Medical Sciences, Faculty of Medicine, Imperial College London, London, UK.ORCID http://orcid.org/0000-0003-2889-3288
Amanda G FisherDepartment of Biochemistry, University of Oxford, Oxford, UK. amanda.fisher@bioch.ox.ac.uk.ORCID http://orcid.org/0000-0003-3010-3644

Funding

RCUK | Medical Research Council (MRC) MC 20027516, MC_UP_1605/12 and MC_UP_1605/11RCUK | Medical Research Council (MRC) MC 22015RCUK | Medical Research Council (MRC) MC PC 23014Wellcome TrustWellcome Trust (Wellcome) WCMA_PSN102
6 · The paper itself

Abstract

In mammals, chromosome-wide regulatory mechanisms ensure a balance of X-linked gene dosage between males (XY) and females (XX). In female cells, expression of genes from one of the two X chromosomes is curtailed, with selective accumulation of Xist-RNA, Xist-associated proteins, specific histone modifications (for example, H3K27me3) and Barr body formation observed throughout interphase. Here we show, using chromosome flow-sorting, that during mitosis, Xist-associated proteins dissociate from inactive X (Xi) chromosomes, while high levels of H3K27me3 and increased compaction of the Xi relative to active X (Xa), are retained. Proteomic comparison of mitotic Xi and Xa revealed that components of Hbo1 and Msl/Mof histone acetyltransferase complexes are significantly enriched on Xa as compared to Xi and autosomes. By contrast, inhibitors of histone acetylation co-enrich with Xi. Furthermore, inhibition of Hbo1 or deletion of Msl/Mof components functionally abolishes mitotic differences in H3K27me3 marking and chromosome compaction. These data uncover critical roles for acetylation pathways in preserving X chromosome properties during mitosis.

Indexed as

Histone AcetyltransferasesHistonesMitosisNuclear ProteinsX ChromosomeX Chromosome InactivationAcetylationAnimalsFemaleHumansMaleMiceProteomicsRNA, Long NoncodingHistone AcetyltransferasesHistonesKat8 protein, mouseNuclear ProteinsRNA, Long NoncodingXIST non-coding RNA

Identifiers

PMID40921734
PMCPMC12431858

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.